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Protein

Arylamine N-acetyltransferase

Gene

nat

Organism
Mycobacterium smegmatis
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the transfer of the acetyl group from acetyl coenzyme A to the free amino group of arylamines and hydrazines. Substrates include isoniazid, anisidine, and 4-aminoveratrole, and to a much lesser extent, p-aminobenzoic acid.2 Publications

Catalytic activityi

Acetyl-CoA + an arylamine = CoA + an N-acetylarylamine.2 Publications

Kineticsi

  1. KM=25 µM for isoniazid1 Publication
  2. KM=300 µM for anisidine1 Publication
  3. KM=650 µM for 4-aminoveratrole1 Publication
  4. KM=87 µM for isoniazid1 Publication
  5. KM=245 µM for 4-anisidine1 Publication
  6. KM=1.42 mM for 4-aminoveratrole1 Publication
  1. Vmax=63 nmol/min/mg enzyme with isoniazid as substrate1 Publication
  2. Vmax=4.8 nmol/min/mg enzyme with anisidine as substrate1 Publication
  3. Vmax=16.2 nmol/min/mg enzyme with 4-aminoveratrole as substrate1 Publication
  4. Vmax=115 nmol/min/mg enzyme with isoniazid as substrate1 Publication
  5. Vmax=114 nmol/min/mg enzyme with 4-anisidine as substrate1 Publication
  6. Vmax=6.5 µmol/min/mg enzyme with 4-aminoveratrole as substrate1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei70Acyl-thioester intermediate2 Publications1
Active sitei1102 Publications1
Active sitei1272 Publications1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Enzyme and pathway databases

BRENDAi2.3.1.5. 3512.

Names & Taxonomyi

Protein namesi
Recommended name:
Arylamine N-acetyltransferase1 Publication (EC:2.3.1.52 Publications)
Short name:
NAT1 Publication
Gene namesi
Name:nat1 Publication
OrganismiMycobacterium smegmatis
Taxonomic identifieri1772 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacterium

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi70C → A, S or Q: Loss of activity. 1 Publication1
Mutagenesisi110H → A, R or W: Loss of activity. 1 Publication1
Mutagenesisi127D → A, N or W: Loss of activity. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL6060.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001079181 – 275Arylamine N-acetyltransferaseAdd BLAST275

Interactioni

Subunit structurei

Homodimer and homotetramer.1 Publication

Protein-protein interaction databases

STRINGi246196.MSMEG_0306.

Chemistry databases

BindingDBiO86309.

Structurei

Secondary structure

1275
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi5 – 11Combined sources7
Helixi22 – 35Combined sources14
Helixi41 – 44Combined sources4
Helixi54 – 61Combined sources8
Turni62 – 64Combined sources3
Helixi70 – 84Combined sources15
Beta strandi87 – 95Combined sources9
Beta strandi108 – 116Combined sources9
Beta strandi120 – 122Combined sources3
Beta strandi124 – 126Combined sources3
Beta strandi139 – 141Combined sources3
Beta strandi143 – 147Combined sources5
Beta strandi150 – 152Combined sources3
Beta strandi154 – 159Combined sources6
Beta strandi162 – 169Combined sources8
Beta strandi172 – 179Combined sources8
Helixi186 – 198Combined sources13
Helixi203 – 206Combined sources4
Beta strandi209 – 213Combined sources5
Beta strandi215 – 222Combined sources8
Beta strandi225 – 230Combined sources6
Beta strandi233 – 241Combined sources9
Helixi242 – 251Combined sources10
Helixi257 – 260Combined sources4
Helixi265 – 271Combined sources7
Turni272 – 274Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1GX3X-ray1.70A/B/C/D1-275[»]
1W5RX-ray1.45A/B1-275[»]
1W6FX-ray2.10A/B/C/D1-275[»]
ProteinModelPortaliO86309.
SMRiO86309.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO86309.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4108MUX. Bacteria.
COG2162. LUCA.

Family and domain databases

InterProiIPR001447. Arylamine_N-AcTrfase.
[Graphical view]
PANTHERiPTHR11786. PTHR11786. 1 hit.
PfamiPF00797. Acetyltransf_2. 1 hit.
[Graphical view]
PRINTSiPR01543. ANATRNSFRASE.

Sequencei

Sequence statusi: Complete.

O86309-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAMDLGGYLT RIGLDGRPRP DLGTLHAIVA AHNRSIPFEN LDPLLGIPVA
60 70 80 90 100
DLSAEALFAK LVDRRRGGYC YEHNGLLGYV LEELGFEVER LSGRVVWMRA
110 120 130 140 150
DDAPLPAQTH NVLSVAVPGA DGRYLVDVGF GGQTLTSPIR LEAGPVQQTR
160 170 180 190 200
HEPYRLTRHG DDHTLAAQVR GEWQPLYTFT TEPRPRIDLE VGSWYVSTHP
210 220 230 240 250
GSHFVTGLTV AVVTDDARYN LRGRNLAVHR SGATEHIRFD SAAQVLDAIV
260 270
NRFGIDLGDL AGRDVQARVA EVLDT
Length:275
Mass (Da):30,174
Last modified:December 1, 2000 - v3
Checksum:iC35800574905D3B9
GO

Sequence cautioni

The sequence CAA07100 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ006588 Genomic DNA. Translation: CAA07100.2. Different initiation.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ006588 Genomic DNA. Translation: CAA07100.2. Different initiation.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1GX3X-ray1.70A/B/C/D1-275[»]
1W5RX-ray1.45A/B1-275[»]
1W6FX-ray2.10A/B/C/D1-275[»]
ProteinModelPortaliO86309.
SMRiO86309.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi246196.MSMEG_0306.

Chemistry databases

BindingDBiO86309.
ChEMBLiCHEMBL6060.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4108MUX. Bacteria.
COG2162. LUCA.

Enzyme and pathway databases

BRENDAi2.3.1.5. 3512.

Miscellaneous databases

EvolutionaryTraceiO86309.

Family and domain databases

InterProiIPR001447. Arylamine_N-AcTrfase.
[Graphical view]
PANTHERiPTHR11786. PTHR11786. 1 hit.
PfamiPF00797. Acetyltransf_2. 1 hit.
[Graphical view]
PRINTSiPR01543. ANATRNSFRASE.
ProtoNetiSearch...

Entry informationi

Entry nameiNAT_MYCSM
AccessioniPrimary (citable) accession number: O86309
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: December 1, 2000
Last modified: November 2, 2016
This is version 89 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.